ID   APC4_PONAB              Reviewed;         817 AA.
AC   Q5RAQ5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Anaphase-promoting complex subunit 4;
DE            Short=APC4;
DE   AltName: Full=Cyclosome subunit 4;
GN   Name=ANAPC4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle. The
CC       APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation of
CC       'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC       formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC       subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC       ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC       ANAPC16 that assemble into a complex of at least 19 chains with a
CC       combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC       and FBXO5. In the context of the APC/C complex, directly interacts with
CC       UBE2S. {ECO:0000250|UniProtKB:Q9UJX5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJX5}.
CC   -!- SIMILARITY: Belongs to the APC4 family. {ECO:0000305}.
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DR   EMBL; CR858957; CAH91155.1; -; mRNA.
DR   RefSeq; NP_001125674.1; NM_001132202.2.
DR   AlphaFoldDB; Q5RAQ5; -.
DR   SMR; Q5RAQ5; -.
DR   STRING; 9601.ENSPPYP00000016367; -.
DR   GeneID; 100172595; -.
DR   KEGG; pon:100172595; -.
DR   CTD; 29945; -.
DR   eggNOG; KOG4399; Eukaryota.
DR   eggNOG; KOG4640; Eukaryota.
DR   InParanoid; Q5RAQ5; -.
DR   OrthoDB; 351579at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR024789; APC4.
DR   InterPro; IPR024790; APC4_long_dom.
DR   InterPro; IPR017169; APC4_metazoa.
DR   InterPro; IPR024977; Apc4_WD40_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13260; PTHR13260; 1.
DR   Pfam; PF12896; ANAPC4; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   PIRSF; PIRSF037303; APC4; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Isopeptide bond; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..817
FT                   /note="Anaphase-promoting complex subunit 4"
FT                   /id="PRO_0000345958"
FT   MOD_RES         469
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT   MOD_RES         757
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT   MOD_RES         777
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT   MOD_RES         779
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT   CROSSLNK        772
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT   CROSSLNK        798
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX5"
SQ   SEQUENCE   817 AA;  92953 MW;  F62798B324A04CDC CRC64;
     MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP
     NENTGKEVTC LAWRPDGKLL AFALADTKKI VLCDVEKPGS LHSFSVEAPV SCMHWMEVTV
     ESSVLTSFYN AEDESNLLLP KLPTLPKNYS STSKIFSEEN SDEIIKLLGD VRLNILVLGG
     SSGFIELYAY GMFKIARVTG IAGTCLALCL SSDLKSLSVV TEVSTNGASE VSYFQLETNL
     LYSFLPEVTR MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKNTTTSV
     QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS HLQSGSESLL
     YHLSELKGLA SWKQKYEPLG LDAAGIEEAI TAVGSFILKA NELLQVIDSS MKNFKAFFRW
     LYVAMLRMTE DHVLPELNKM TQKDITFVAE FLTEHFNEAP DLYNRKGKYF NVERVGQYLK
     DEDDDLVSPP NTEGNQWYDF LQNSSHLKES PLLFPYYPRK SLHFVKRRME NIIDQCLQKP
     ADVIGKSMNQ AICIPLYRDT RSEDSIRRLF KFPFLWNNKT SNLHYLLFTI LEDSLYKMCI
     LRRHTDISQS VSNGLIAIKF GSFTYATTEK VRRSIYSCLD AQFYDDETVT VVLKDTVGRE
     GRDRLLVQLP LSLVYNSEDS AEYQFTGTYS TRLDEQCSAI PTRTMHFEKH WRLLESMKAQ
     YVAGNGFRKV SCVLSSNLRH VRVFEMDIDD EWELDESSDE EEEASNKPVK IKEEVLSESE
     AENQQAGAAA LAPEIVIKVE KLDPELDSQS SLPLLCV